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. 2010 Dec 1;21(23):4212–4226. doi: 10.1091/mbc.E10-04-0287

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© 2010 by The American Society for Cell Biology

This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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Figure 6. — Quantitative immunoprecipitation of RRP1B selectively enriches molecular complexes containing 60S (RPL) proteins and pre-60S ribosomal subunit processing proteins. (A) Design of a typical quantitative SILAC IP experiment. (B) Real hits are distinguished by their high SILAC ratios (>1), which shift them from the bell curve distribution of contaminants (ratio of ∼1). Plotting log SILAC ratio versus relative peptide intensity highlights the RPLs and pre-60S processing proteins purified with both endogenous nuclear RRP1B (C) and GFP-tagged nucleolar PP1γ (D).